ID A0A365YX82_9ACTN Unreviewed; 330 AA.
AC A0A365YX82;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:RBM06881.1};
GN ORFNames=DEH69_25815 {ECO:0000313|EMBL:RBM06881.1};
OS Streptomyces sp. PT12.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1510197 {ECO:0000313|EMBL:RBM06881.1, ECO:0000313|Proteomes:UP000252839};
RN [1] {ECO:0000313|EMBL:RBM06881.1, ECO:0000313|Proteomes:UP000252839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PT12 {ECO:0000313|EMBL:RBM06881.1,
RC ECO:0000313|Proteomes:UP000252839};
RA Devaraj K., Tan G.Y.A.;
RT "Diversity of actinobacteria isolated from Cape Rachado, Malaysia.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBM06881.1}.
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DR EMBL; QEST01000236; RBM06881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365YX82; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000252839; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12167; 2-Hacid_dh_8; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000252839}.
FT DOMAIN 52..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 138..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 35434 MW; 11BC3BB78458F366 CRC64;
MSPRRPVTTI AMDPRVAARL INAPLRERLR TIADVQPAHV VSDFTGVELA HTEVLFTSWG
CPPVTAEVLA RAPRLRAIVH AAGTVKELVT DACWRRGIAV SSAAAANAEP VAEYTLAAIL
FSGKRVMDIA RAYRHFPAAD DWAARFPGLG NYRRTVGVVG ASRIGRRVIE LLRPFTLDVL
VSDPYLDEEL PGARRVDLDE LLASSDIVTL HAPALPETHH MIDAARLASM PDGATLINTA
RAALVDQEAL IAELASGRLY AVLDLTQPEV LPASSPLHDL PNVLVTPHIA GSLGGELARM
ADLALDELAR HAHGLPFIHP VDPTTLARSA
//
